Cloned (Comment) | Organism |
---|---|
- |
Chloracidobacterium thermophilum |
Crystallization (Comment) | Organism |
---|---|
to 2.5 A resolution. Enzyme is a tetramer. The active site is located at the interface between the N- and C-terminal domains for each monomer where a mononuclear nonheme iron is coordinated by His62, His153, His157 and three water molecules in an octahedral arrangement | Chloracidobacterium thermophilum |
Protein Variants | Comment | Organism |
---|---|---|
A420Y | position is involved in controlling the reaction selectiviy. Mutant leads to an increased amount of side-reaction (cysteine dioxygenase activity) | Chloracidobacterium thermophilum |
D52L | mutation may disrupt the hydrogen bond between Asp52 and glutamyl group of substrate gamma-Glu-Cys, which in turn alters the substrate selectivity | Chloracidobacterium thermophilum |
D52L/A420Y | mutation tunes EgtB activity toward Egt1-type, i.e. reaction of EC 1.21.3.10 | Chloracidobacterium thermophilum |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.013 | - |
hercynine | mutant A420Y, pH not specified in the publication, temperature not specified in the publication | Chloracidobacterium thermophilum | |
0.015 | - |
hercynine | mutant D52L/A420Y, pH not specified in the publication, temperature not specified in the publication | Chloracidobacterium thermophilum | |
0.02 | - |
hercynine | mutant D52L, pH not specified in the publication, temperature not specified in the publication | Chloracidobacterium thermophilum | |
0.041 | - |
hercynine | pH not specified in the publication, temperature not specified in the publication | Chloracidobacterium thermophilum | |
3.1 | - |
gamma-L-glutamyl-L-cysteine | mutant A420Y, pH not specified in the publication, temperature not specified in the publication | Chloracidobacterium thermophilum | |
3.9 | - |
gamma-L-glutamyl-L-cysteine | mutant D52L, pH not specified in the publication, temperature not specified in the publication | Chloracidobacterium thermophilum | |
4.2 | - |
gamma-L-glutamyl-L-cysteine | mutant D52L/A420Y, pH not specified in the publication, temperature not specified in the publication | Chloracidobacterium thermophilum | |
5.9 | - |
gamma-L-glutamyl-L-cysteine | wild-type, pH not specified in the publication, temperature not specified in the publication | Chloracidobacterium thermophilum |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Iron | protein conatains 0.92 iron per monomer. A mononuclear nonheme iron is coordinated by His62, His153, His157 and three water molecules in an octahedral arrangement | Chloracidobacterium thermophilum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Chloracidobacterium thermophilum | G2LET6 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
hercynine + gamma-L-glutamyl-L-cysteine + O2 | - |
Chloracidobacterium thermophilum | gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O | - |
? | |
additional information | enzyme additionally accepts L-cysteine, i.e. reaction of EC 1.21.3.10 | Chloracidobacterium thermophilum | ? | - |
- |
Synonyms | Comment | Organism |
---|---|---|
Cabther_A1318 | - |
Chloracidobacterium thermophilum |
EgtB | - |
Chloracidobacterium thermophilum |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.22 | - |
hercynine | mutant D52L, pH not specified in the publication, temperature not specified in the publication | Chloracidobacterium thermophilum | |
0.29 | - |
hercynine | wild-type, pH not specified in the publication, temperature not specified in the publication | Chloracidobacterium thermophilum | |
0.29 | - |
hercynine | mutant A420Y, pH not specified in the publication, temperature not specified in the publication | Chloracidobacterium thermophilum | |
0.31 | - |
hercynine | mutant D52L/A420Y, pH not specified in the publication, temperature not specified in the publication | Chloracidobacterium thermophilum |
General Information | Comment | Organism |
---|---|---|
physiological function | EgtB of Candidatus Chloracidobacterium thermophilum has both EgtB- and Egt1-type of activities, i.e. reactions of EC 1.14.99.50 and EC 1.21.3.10 | Chloracidobacterium thermophilum |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.05 | - |
gamma-L-glutamyl-L-cysteine | wild-type, pH not specified in the publication, temperature not specified in the publication | Chloracidobacterium thermophilum | |
0.055 | - |
gamma-L-glutamyl-L-cysteine | mutant D52L, pH not specified in the publication, temperature not specified in the publication | Chloracidobacterium thermophilum | |
0.073 | - |
gamma-L-glutamyl-L-cysteine | mutant D52L/A420Y, pH not specified in the publication, temperature not specified in the publication | Chloracidobacterium thermophilum | |
0.09 | - |
gamma-L-glutamyl-L-cysteine | mutant A420Y, pH not specified in the publication, temperature not specified in the publication | Chloracidobacterium thermophilum | |
7 | - |
hercynine | pH not specified in the publication, temperature not specified in the publication | Chloracidobacterium thermophilum | |
11 | - |
hercynine | mutant D52L, pH not specified in the publication, temperature not specified in the publication | Chloracidobacterium thermophilum | |
20 | - |
hercynine | mutant D52L/A420Y, pH not specified in the publication, temperature not specified in the publication | Chloracidobacterium thermophilum | |
21.7 | - |
hercynine | mutant A420Y, pH not specified in the publication, temperature not specified in the publication | Chloracidobacterium thermophilum |